ID MURA1_STRPI Reviewed; 419 AA. AC B1IBM3; DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00111}; DE EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111}; DE AltName: Full=Enoylpyruvate transferase {ECO:0000255|HAMAP-Rule:MF_00111}; DE Short=EPT {ECO:0000305}; DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000255|HAMAP-Rule:MF_00111}; GN Name=murA1 {ECO:0000312|EMBL:ACA37082.1}; GN Synonyms=murA {ECO:0000255|HAMAP-Rule:MF_00111}; GN OrderedLocusNames=SPH_1173 {ECO:0000312|EMBL:ACA37082.1}; OS Streptococcus pneumoniae (strain Hungary19A-6). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=487214 {ECO:0000312|EMBL:ACA37082.1}; RN [1] {ECO:0000312|Proteomes:UP000002163} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hungary19A-6 {ECO:0000312|Proteomes:UP000002163}; RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107; RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J., RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R., RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D., RA Rappuoli R., Moxon E.R., Masignani V.; RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and RT closely related species."; RL Genome Biol. 11:R107.1-R107.19(2010). RN [2] {ECO:0007744|PDB:3ZH4} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION, AND MISCELLANEOUS. RC STRAIN=Hungary19A-6 {ECO:0000303|PubMed:23571543}; RX PubMed=23571543; DOI=10.1128/aac.00223-13; RA Engel H., Gutierrez-Fernandez J., Fluckiger C., Martinez-Ripoll M., RA Muhlemann K., Hermoso J.A., Hilty M., Hathaway L.J.; RT "Heteroresistance to fosfomycin is predominant in Streptococcus pneumoniae RT and depends on the murA1 gene."; RL Antimicrob. Agents Chemother. 57:2801-2808(2013). CC -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N- CC acetylglucosamine (By similarity). Target for the antibiotic CC fosfomycin. {ECO:0000255|HAMAP-Rule:MF_00111, CC ECO:0000269|PubMed:23571543}. CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = CC phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine; CC Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705, CC ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00111}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- MISCELLANEOUS: This strain of S.pneumoniae has no heteroresistance to CC fosfomycin unlike other strains of this bacterium in which MurA1 is CC required for heteroresistance along with other as yet unknown CC factor(s). Heteroresistance is the ability of a clonal population to CC grow one or several subpopulations at a frequency of 10(-7) to 10(-3) CC in the presence of a higher antibiotic concentration than that CC predicted to be effective by measurement of the minimum inhibitory CC concentration (MIC). {ECO:0000269|PubMed:23571543}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00111}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000936; ACA37082.1; -; Genomic_DNA. DR RefSeq; WP_001227085.1; NC_010380.1. DR PDB; 3ZH4; X-ray; 1.80 A; A=1-419. DR PDBsum; 3ZH4; -. DR AlphaFoldDB; B1IBM3; -. DR SMR; B1IBM3; -. DR GeneID; 66806189; -. DR KEGG; spv:SPH_1173; -. DR HOGENOM; CLU_027387_0_0_9; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000002163; Chromosome. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; ISS:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; ISS:UniProtKB. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro. DR CDD; cd01555; UdpNAET; 1. DR Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2. DR HAMAP; MF_00111; MurA; 1. DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom. DR InterPro; IPR036968; Enolpyruvate_Tfrase_sf. DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. DR InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA. DR NCBIfam; TIGR01072; murA; 1. DR PANTHER; PTHR43783; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1. DR PANTHER; PTHR43783:SF2; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE 2; 1. DR Pfam; PF00275; EPSP_synthase; 1. DR SUPFAM; SSF55205; EPT/RTPC-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Cytoplasm; Peptidoglycan synthesis; KW Pyruvate; Transferase. FT CHAIN 1..419 FT /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase" FT /id="PRO_0000436447" FT ACT_SITE 116 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111" FT BINDING 22..23 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0000250|UniProtKB:P0A749" FT BINDING 92 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000250|UniProtKB:P0A749" FT BINDING 121..125 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000250|UniProtKB:P0A749" FT BINDING 306 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000250|UniProtKB:P0A749" FT BINDING 328 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000250|UniProtKB:P0A749" FT MOD_RES 116 FT /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00111" FT STRAND 3..7 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 12..17 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 22..31 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 32..34 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 39..43 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 48..59 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 63..67 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 70..74 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 75..77 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 92..95 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 96..105 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 122..132 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 139..148 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 165..175 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 178..185 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 191..202 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 212..218 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 226..229 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 234..247 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 248..255 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 258..260 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 262..271 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 275..277 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 279..284 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 308..315 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 318..325 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 327..329 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 335..341 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 346..349 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 352..356 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 365..367 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 371..383 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 384..391 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 394..397 FT /evidence="ECO:0007829|PDB:3ZH4" FT HELIX 403..408 FT /evidence="ECO:0007829|PDB:3ZH4" FT TURN 409..411 FT /evidence="ECO:0007829|PDB:3ZH4" FT STRAND 413..417 FT /evidence="ECO:0007829|PDB:3ZH4" SQ SEQUENCE 419 AA; 45055 MW; A217CD0CB16DF8F9 CRC64; MRKIVINGGL PLQGEITISG AKNSVVALIP AIILADDVVT LDCVPDISDV ASLVEIMELM GATVKRYDDV LEIDPRGVQN IPMPYGKINS LRASYYFYGS LLGRFGEATV GLPGGCDLGP RPIDLHLKAF EAMGATASYE GDNMKLSAKD TGLHGASIYM DTVSVGATIN TMIAAVKANG RTIIENAARE PEIIDVATLL NNMGAHIRGA GTNIIIIDGV ERLHGTRHQV IPDRIEAGTY ISLAAAVGKG IRINNVLYEH LEGFIAKLEE MGVRMTVSED SIFVEEQSNL KAINIKTAPY PGFATDLQQP LTPLLLRANG RGTIVDTIYE KRVNHVFELA KMDADISTTN GHILYTGGRD LRGTSVKATD LRAGAALVIA GLMAEGKTEI TNIEFILRGY SDIIEKLRNL GADIRLVED //